Synthesis and Secondary Structure of Alternate α,β‐Hybrid Peptides Containing Oxazolidin‐2‐one Moieties

Angelici, Gaetano; Luppi, Gianlugi; Kaptein, Bernard; Broxterman, Quirinus B.; Hofmann, Hans‐Jörg; Tomasini, Claudia

doi:10.1002/ejoc.200700134

Cited by 42 publications

(17 citation statements)

References 65 publications

(14 reference statements)

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“…The sign of the band at 460 nm indicates the preferential helicity adopted by the Fc moiety, which is normally controlled by one or more intramolecular hydrogen bonds (as it occurs in 1,1′‐disubstituted Fc) . In our case, the X‐ray structure of 1 (Figures and ) features an H···π interaction between one cyclopentadienyl (Cp) and the adjacent Phe ring which may be responsible for the chirality transfer to the Fc.…”

Section: Resultsmentioning

confidence: 69%

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Synthesis and structure analysis of ferrocene‐containing pseudopeptides

et al. 2018

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Ferrocene with its aromaticity and facile redox properties is an attractive moiety to be incorporated into functional moieties. Medicinal applications of ferrocene are well known and ferrocene itself shows cytotoxic and antianemic properties. In this article, we will describe the synthesis and the structure analysis of two pseudopeptides containing a ferrocene moiety as N-terminal group. After purification, Fc-l-Phe-d-Oxd-OBn [l-Phel-phenylalanine; d-Oxd(4R,5S)-4-Methyl-5-carboxy-oxazolidin-2-one] appears as bright brown solid that spontaneously forms brown needles. The X-ray diffraction of the crystals shows the presence of strong π interactions between the ferrocenyl moiety and the phenyl rings, while no NH•••OC hydrogen bonds are formed. This result is confirmed by FT-IR and H NMR analysis. In contrast, both FT-IR and H NMR analysis suggest that Fc-(l-Phe-d-Oxd) -OBn forms a turn conformation stabilized by intramolecular NH•••OC hydrogen bonds in solution. Chiroptical spectroscopies (ECD and VCD) substantially confirmed the absence of a well-defined folded structure. The presence of the Fc moiety is responsible for specific ECD signals, one of which displayed pronounced temperature dependence and is directly related with the helicity assumed by the Fc core. Solid-state ECD spectra were recorded and rationalized on the basis of the X-ray geometry and quantum-mechanical calculations.

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Section: Resultsmentioning

confidence: 69%

“…The two pseudopeptides are oligomers containing the l ‐Phe‐ d ‐Oxd unit, that is a privileged scaffold for the formation of supramolecular materials . d ‐Oxd mimics a proline group and may form oligomers having stable secondary structures in solution, due to its ability to block the peptide bond always in the trans conformation …”

Section: Resultsmentioning

confidence: 99%

Synthesis and structure analysis of ferrocene‐containing pseudopeptides

et al. 2018

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“…Nearly 10 years ago we found out that our 4‐methyl‐5‐carboxy‐oxazolidin‐2‐one moiety (that we will call Oxd from now on) could be successfully utilized in the formation of supramolecular materials. This little molecule, that mimics a proline group, may form oligomers having stable secondary structures in solution, due to its ability to block the peptide bond always in the trans conformation . This outcome does not take place in the prolyl bonds that can also adopt the cis conformation …”

Section: Introductionmentioning

confidence: 99%

Oxazolidinone‐containing pseudopeptides: Supramolecular materials, fibers, crystals, and gels

Tomasini

Zanna

2017

Biopolymers

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The formation of fibers through self-assembly is of particular interest, as fibrous proteins (such as collagen, keratin, actin, and so on) are involved in intra- and extracellular functions. To understand aggregation phenomena, oligopeptides may be designed and prepared either to mimic or to interfere with these processes. In this article, we will demonstrate that the introduction of the 4-methyl-5-carboxy-oxazolidin-2-one (Oxd) moiety inside a peptide chain favors the formation of fiber-like materials organized either in β-sheets or in supramolecular helices, provided that it is combined with other factors, like π-stacking interactions and intermolecular NH•••OC bonds. The presence of the Oxd moiety is essential for the material formation: when Oxd is replaced with Pro, only liquids or amorphous solids are obtained. Remarkably, some of these molecules are low-molecular-weight gelators, as they induce the formation of both organogel and hydrogels that have been used for several applications.

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“…Based on the number of atoms involved in the H‐bonding pseudocycle the β‐ and γ‐peptide helices are classified as C 9 ‐, C 10 ‐, C 12 ‐, C 13 ‐, C 14 ‐helices etc . Further, the hybrid peptides composed of α‐, β‐, and γ‐amino acids displayed a variety of helices with different H‐bonding patterns . Both theoretical and experimental investigations revealed the stable 12‐helical conformations from the α, γ‐hybrid peptides composed of 1:1 alternating α‐ and γ‐amino acids.…”

Section: Introductionmentioning

confidence: 99%

Helices with additional H‐bonds: crystallographic conformations of α,γ‐hybrid peptides helices composed of β‐hydroxy γ‐amino acids (statines)

et al. 2017

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β-Hydroxy-γ-amino acids (Statines) are a class of naturally occurring non-ribosomal amino acids frequently found in many peptide natural products. Peptidomimetics constituted with statines have been used as inhibitors for various aspartic acid proteases. In contrast to the synthetic γ-amino acids, very little is known about the folding behavior of these naturally occurring β-hydroxy γ-amino acids. To understand the folding behavior of statines, three α,γ-hybrid peptides P1 (Ac-Aib-γPhe-Aib-(R, S)Phesta-Aib-γPhe-Aib-CONH ), P2 (Ac-Aib-γPhe-Aib-(S, S)Phesta-Aib-γPhe-Aib-CONH ), and P3 (Ac-Aib-γPhe-Aib-(S, S)Phesta-Aib-(S, S)Phesta-Aib-CONH ) were synthesized on solid phase and their helical conformations in single crystals were studied. Results suggest that both syn and anti diastereoisomers of statines can be accommodated into the helix without deviating overall helical conformation of α,γ-hybrid peptides. In comparison with syn diastereoisomer, the anti diastereoisomer was found to be directly involved in the intramolecular H-bonding with the backbone carbonyl groups (i to i + 3) similar to the backbone amide NHs in the helix.

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Synthesis and Secondary Structure of Alternate α,β‐Hybrid Peptides Containing Oxazolidin‐2‐one Moieties

Cited by 42 publications

References 65 publications

Synthesis and structure analysis of ferrocene‐containing pseudopeptides

Synthesis and structure analysis of ferrocene‐containing pseudopeptides

Oxazolidinone‐containing pseudopeptides: Supramolecular materials, fibers, crystals, and gels

Helices with additional H‐bonds: crystallographic conformations of α,γ‐hybrid peptides helices composed of β‐hydroxy γ‐amino acids (statines)

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